The Ribosomal Peptidyl Transferase.
From: Institute of Physical Biochemistry, University of Witten/Herdecke, Witten, Germany.
Molecular cell
- Publish Date: May 2007
- ISSN: 1097-2765
- Volume: 26
- Issue: 3
- Pages: 311-21
- Medium: Print
- Language: English
- Citation (JAMA): Beringer Malte, Rodnina Marina V, et al. The Ribosomal Peptidyl Transferase.. Mol. Cell May 2007;26:311-21
Abstract
Peptide bond formation on the ribosome takes place in an active site composed of RNA. Recent progress of structural, biochemical, and computational approaches has provided a fairly detailed picture of the catalytic mechanism of the reaction. The ribosome accelerates peptide bond formation by lowering the activation entropy of the reaction due to positioning the two substrates, ordering water in the active site, and providing an electrostatic network that stabilizes the reaction intermediates. Proton transfer during the reaction appears to be promoted by a concerted proton shuttle mechanism that involves ribose hydroxyl groups on the tRNA substrate.
Mesh Headings (Keywords): Bacteria, Base Sequence, Binding Sites, Catalysis, Crystallization, Models, Molecular, Peptidyl Transferases, Protein Biosynthesis, Protein Conformation, RNA, Ribosomal, RNA, Transfer, Ribosomal Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 17499039
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.